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Nanozeolite-coupled biochar fertilizer may help bamboo forest soils hold on to carbon under warming

Researchers found that nanozeolite-coupled biochar fertilizer reduced soil-derived carbon dioxide emissions by 11-18% compared to conventional phosphorus fertilizer. The biochar-based fertilizer also reduced the Q10 value, indicating a decrease in soil carbon decomposition under warming.

SourceBiochar Editorial Office, Shenyang Agricultural University·JournalBiochar·TypeExperimental study·DateJun 16, 2026

Proteins cluster in cells for faster performance

Researchers at the University of Groningen discovered that protein clustering in cells leads to reduced movement and improved efficiency in amino acid production. This finding has practical implications for designing efficient cell factories and increasing substance production inside cells.

SourceUniversity of Groningen·JournalMolecular Cell·TypeExperimental study·DateApr 13, 2026

Researchers decode molecular secrets of surfactant-mediated enzyme protection in lignocellulose biorefining

A comprehensive study decodes structure-function relationships governing surfactant-mediated enzyme protection, revealing a competitive stabilization mechanism. The research identifies key factors influencing mitigation efficacy, including hydrophobicity and hydrogen bonding capacity, and provides predictive power for designing more ef...

SourceJournal of Bioresources and Bioproducts·JournalJournal of Bioresources and Bioproducts·DateMar 31, 2026

Not just sweet: the sugar branches that shape the brain

A brain-specific enzyme reshapes protein-linked sugar chains to facilitate the formation of complex glycans essential for normal brain function. This process is critical for efficient keratan sulfate formation and has implications for research into glycan-related brain disorders.

SourceInstitute for Glyco-core Research (iGCORE), Tokai National Higher Education and Research System·JournalJournal of Biological Chemistry·TypeExperimental study·DateJan 26, 2026

New AI method revolutionizes the design of enzymes

Researchers have developed a new AI method called Riff-Diff to construct artificial biocatalysts, resulting in enzymes that are significantly faster, more stable and versatile. The technology allows for precise design of protein structures around active centres, making enzyme design more accessible to the wider biotechnology community.

SourceGraz University of Technology·JournalNature·TypeComputational simulation/modeling·DateJan 22, 2026

An enzyme neutralizes pathogens by cleaving a bacterial toxin

Scientists at Leibniz-HKI discovered an enzyme called BurK that cleaves the toxic molecule malleicyprol in human pathogenic bacteria. This mechanism regulates toxin levels and renders it harmless to humans, offering a potential therapeutic approach for antibiotic-resistant infections.

Novel AI method sheds light on how enzyme linked to Alzheimer’s selects its targets

A novel AI-based approach identifies a distinct physicochemical signature near the cleavage site of gamma-secretase substrates, revealing dynamic properties essential for molecular recognition. The study highlights the potential of this methodology to improve understanding of gamma-secretase's role in diseases and aid drug development.

SourceDZNE - German Center for Neurodegenerative Diseases·JournalNature Communications·TypeComputational simulation/modeling·DateJul 9, 2025

Research opens up new avenue for Tuberculosis drug discovery

Scientists from the University of Bath have identified two new families of chemical compounds that inhibit alpha-methylacyl-CoA racemase (MCR) in Mycobacterium tuberculosis, a key enzyme for TB survival. This breakthrough could lead to new treatments for TB and potentially other diseases like prostate cancer.

SourceUniversity of Bath·JournalJournal of Biological Chemistry·TypeExperimental study·DateJul 2, 2025

A new complexity in protein chemistry

Göttingen University researchers have discovered previously undetected chemical bonds within archived protein structures, revealing an unexpected complexity in protein chemistry. These newly identified nitrogen-oxygen-sulphur (NOS) linkages broaden our understanding of how proteins respond to oxidative stress.

SourceUniversity of Göttingen·JournalCommunications Chemistry·TypeComputational simulation/modeling·DateMay 20, 2025

The evolution of low-temperature adapted enzymes

Researchers used ancestral sequence reconstruction to study the evolution of enzyme thermostability and cold adaptation. They identified key amino acid substitutions that enhanced catalytic activity at low temperatures, revealing a structural shift between intermediate ancestral enzymes.

SourceWaseda University·JournalProtein Science·TypeExperimental study·DateMar 25, 2025

Glycans can regulate their own biosynthesis by modifying enzyme activity

Researchers found that glycans attached to glycosylation enzymes' lectin domains inhibit the enzymes' activity, leading to self-regulation of their own biosynthesis. This unique mechanism sheds light on how glycosylation enzymes choose their substrate proteins in cells.

Biologists uncover how key carbohydrate-attachment mechanism malfunctions

Biologists discovered a key enzyme's interaction with a small structure in glycans that contributes to the malfunctioning of carbohydrates' attachment process. This process is essential for numerous physiological processes and can lead to diseases such as cancer, diabetes, Alzheimer's, and muscular dystrophy.

SourceInstitute for Glyco-core Research (iGCORE), Tokai National Higher Education and Research System·JournalJournal of Biological Chemistry·TypeExperimental study·DateJun 26, 2024

Marine bacteria take a bite at plastic pollution

Researchers at Hokkaido University found a bacterium that can break down the eco-friendly polymer polybutylene succinate in marine environments. The discovery of the enzyme PBSase has the potential to improve recycling technologies and develop new marine biodegradable polymers.

SourceHokkaido University·JournalEnvironmental Microbiology·TypeExperimental study·DateOct 16, 2023

New enzyme could aid anticancer drug development

A new enzyme, CtdY, has been identified that can break an amide bond, a fundamental type of bond found in proteins. This discovery holds significant promise for the pharmaceutical industry, as it could enable the creation of new anticancer drugs and improve treatment outcomes.

SourceRice University·JournalJournal of the American Chemical Society·TypeExperimental study·DateJun 27, 2023

Research team from Goethe University discovers Achilles’ heel of dangerous hospital pathogen

A team from Goethe University has identified the spatial structure of the mannitol-synthesizing enzyme MtlD in Acinetobacter baumannii, which is crucial for its survival. This discovery could lead to the development of customized substances to inhibit the enzyme and combat this hospital pathogen.

SourceGoethe University Frankfurt·JournalProceedings of the National Academy of Sciences·TypeExperimental study·DateApr 6, 2022

Making patient care easier: Self-powered diaper sensors that monitor urine sugar levels

Researchers from Tokyo University of Science developed a self-powered diaper sensor that monitors urine sugar levels, providing an alternative biomarker for blood sugar monitoring. The sensor uses a biofuel cell powered by glucose in the urine, detecting sugar levels within 1 second and simplifying caretaking tasks.

SourceTokyo University of Science·JournalACS Sensors·TypeExperimental study·DateAug 23, 2021